Jermy AJ, et al. (2006) The Brl domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons. J Biol Chem 281(12):7899-906
Abstract: Protein translocation into the endoplasmic reticulum (ER) occurs at pore-forming structures known as translocons. In yeast, two different targeting pathways converge at a translocation pore formed by the Sec61-complex. The SRP-dependent pathway targets nascent precursors co-translationally, while the Sec62p-dependent pathway targets polypeptides post-translationally. In addition to the Sec61-complex, both pathways also require Sec63p, an integral membrane protein of the Hsp40 family, and Kar2p, a soluble Hsp70 located in the ER lumen. Using a series of mutant alleles we demonstrate that a conserved Brl domain (Brr2-like) in the c-terminal cytosolic region of Sec63p is essential for function both in vivo and in vitro. We further demonstrate that this domain is required for assembly of two oligomeric complexes of 350 and 380 kDa respectively. The larger of these corresponds to the heptameric "SEC-complex" required for post-translational translocation. However, the 350 kDa complex represents a newly defined hexameric SEC' complex comprising Sec61p, Sss1p, Sbh1p, Sec63p, Sec71p and Sec72p. Our data indicate that the SEC' complex is required for co-translational protein translocation across the yeast ER membrane.
|Status: Published||Type: Journal Article||PubMed ID: 16368690|
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